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Volumn 7, Issue 7, 2008, Pages 3028-3034

A shotgun proteomic method for the identification of membrane-embedded proteins and peptides

Author keywords

Cyanogen bromide; Integral membrane proteins; Mass spectrometry; Membrane shaving; MudPIT; Proteinase K; Proteomics; Transmembrane domains

Indexed keywords

INTEGRAL MEMBRANE PROTEIN; MEMBRANE PROTEIN; UNCLASSIFIED DRUG; PEPTIDE; PROTEINASE K;

EID: 51649102828     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr700795f     Document Type: Article
Times cited : (39)

References (27)
  • 1
    • 34548202704 scopus 로고    scopus 로고
    • Proteomics of integral membrane proteins-theory and application
    • Speers, A. E.; Wu, C. C. Proteomics of integral membrane proteins-theory and application. Chem Rev 2007, 107 (8), 3687-3714.
    • (2007) Chem Rev , vol.107 , Issue.8 , pp. 3687-3714
    • Speers, A.E.1    Wu, C.C.2
  • 3
    • 34547232157 scopus 로고    scopus 로고
    • Optimization of mass spectrometry-compatible surfactants for shotgun proteomics
    • Chen, E. I.; Cociorva, D.; Norris, J. L.; Yates, J. R., III. Optimization of mass spectrometry-compatible surfactants for shotgun proteomics. J. Proteome Res. 2007, 6 (7), 2529-2538.
    • (2007) J. Proteome Res , vol.6 , Issue.7 , pp. 2529-2538
    • Chen, E.I.1    Cociorva, D.2    Norris, J.L.3    Yates III, J.R.4
  • 4
    • 0942276251 scopus 로고    scopus 로고
    • A detergent- and cyanogen bromide-free method for integral membrane proteomics: Application to Haiobacterium purple membranes and the human epidermal membrane proteome
    • Blonder, J.; Conrads, T. P.; Yu, L. R.; Terunuma, A.; Janini, G. M.; Issaq, H. J.; Vogel, J. C.; Veenstra, T. D. A detergent- and cyanogen bromide-free method for integral membrane proteomics: application to Haiobacterium purple membranes and the human epidermal membrane proteome. Proteomics 2004, 4 (1), 31-45.
    • (2004) Proteomics , vol.4 , Issue.1 , pp. 31-45
    • Blonder, J.1    Conrads, T.P.2    Yu, L.R.3    Terunuma, A.4    Janini, G.M.5    Issaq, H.J.6    Vogel, J.C.7    Veenstra, T.D.8
  • 5
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn, M. P.; Wolters, D.; Yates, I. R., III. Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat. Biotechnol. 2001, 19, 242.
    • (2001) Nat. Biotechnol , vol.19 , pp. 242
    • Washburn, M.P.1    Wolters, D.2    Yates III, I.R.3
  • 6
    • 0038561131 scopus 로고    scopus 로고
    • A method for the comprehensive proteomic analysis of membrane proteins
    • Wu, C. C.; MacCoss, M. J.; Howell, K. E.; Yates, J. R., III. A method for the comprehensive proteomic analysis of membrane proteins. Nat. Biotechnol. 2003, 21 (5), 532-538.
    • (2003) Nat. Biotechnol , vol.21 , Issue.5 , pp. 532-538
    • Wu, C.C.1    MacCoss, M.J.2    Howell, K.E.3    Yates III, J.R.4
  • 7
    • 0020071663 scopus 로고
    • Hepatic Golgi fractions resolved into membrane and content subtractions
    • Howell, K. E.; Palade, G. E. Hepatic Golgi fractions resolved into membrane and content subtractions. J. Cell Biol. 1982, 92 (3), 822- 832.
    • (1982) J. Cell Biol , vol.92 , Issue.3 , pp. 822-832
    • Howell, K.E.1    Palade, G.E.2
  • 9
    • 0442276416 scopus 로고    scopus 로고
    • Structural features of transmembrane helices
    • Hildebrand, P. W.; Preissner, R.; Frommel, C. Structural features of transmembrane helices. FEBS Lett. 2004, 559 (1-3), 145-151.
    • (2004) FEBS Lett , vol.559 , Issue.1-3 , pp. 145-151
    • Hildebrand, P.W.1    Preissner, R.2    Frommel, C.3
  • 10
    • 10944249586 scopus 로고    scopus 로고
    • Hiding behind hydrophobicity. Transmembrane segments in mass spectrometry
    • Eichacker, L. A.; Granvogl, B.; Mirus, O.; Muller, B. C.; Miess, C.; Schleiff, E. Hiding behind hydrophobicity. Transmembrane segments in mass spectrometry. J. Biol. Chem. 2004, 279 (49), 50915- 50922.
    • (2004) J. Biol. Chem , vol.279 , Issue.49 , pp. 50915-50922
    • Eichacker, L.A.1    Granvogl, B.2    Mirus, O.3    Muller, B.C.4    Miess, C.5    Schleiff, E.6
  • 12
    • 0026772657 scopus 로고
    • Sequence analysis of photoaffinity-labelled peptides derived by proteolysis of photosystem-2 reaction centres from thylakoid membranes treated with [14C]azidoatrazine
    • Whitelegge, J. P.; Jewess, P.; Pickering, M. G.; Gerrish, C.; Camilleri, P.; Bowyer, J. R. Sequence analysis of photoaffinity-labelled peptides derived by proteolysis of photosystem-2 reaction centres from thylakoid membranes treated with [14C]azidoatrazine. Eur. J. Biochem. 1992, 207 (3), 1077-1084.
    • (1992) Eur. J. Biochem , vol.207 , Issue.3 , pp. 1077-1084
    • Whitelegge, J.P.1    Jewess, P.2    Pickering, M.G.3    Gerrish, C.4    Camilleri, P.5    Bowyer, J.R.6
  • 13
    • 34347234182 scopus 로고    scopus 로고
    • Shotgun analysis of integral membrane proteins facilitated by elevated temperature
    • Speers, A. E.; Blackler, A. R.; Wu, C. C. Shotgun analysis of integral membrane proteins facilitated by elevated temperature. Anal. Chem. 2007, 79 (12), 4613-4620.
    • (2007) Anal. Chem , vol.79 , Issue.12 , pp. 4613-4620
    • Speers, A.E.1    Blackler, A.R.2    Wu, C.C.3
  • 14
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • Krogh, A.; Larsson, B.; von Heijne, G.; Sonnhammer, E. L. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol. 2001, 305 (3), 567- 580.
    • (2001) J. Mol. Biol , vol.305 , Issue.3 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    von Heijne, G.3    Sonnhammer, E.L.4
  • 15
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J.; Doolittle, R. F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 1982, 157 (1), 105- 132.
    • (1982) J. Mol. Biol , vol.157 , Issue.1 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 16
    • 29144515403 scopus 로고    scopus 로고
    • Families of membranous proteins can be characterized by the amino acid composition of their transmembrane domains
    • Sadka, T.; Linial, M. Families of membranous proteins can be characterized by the amino acid composition of their transmembrane domains. Bioinformatics 2005, 21 (Suppl. 1), 1378-386.
    • (2005) Bioinformatics , vol.21 , Issue.SUPPL. 1 , pp. 1378-1386
    • Sadka, T.1    Linial, M.2
  • 17
    • 33645466243 scopus 로고    scopus 로고
    • Toward the complete membrane proteome: High coverage of integral membrane proteins through transmembrane peptide detection
    • Fischer, F.; Wolters, D.; Rogner, M.; Poetsch, A. Toward the complete membrane proteome: high coverage of integral membrane proteins through transmembrane peptide detection. Mol. Cell. Proteomics 2006, 5 (3), 444-453.
    • (2006) Mol. Cell. Proteomics , vol.5 , Issue.3 , pp. 444-453
    • Fischer, F.1    Wolters, D.2    Rogner, M.3    Poetsch, A.4
  • 18
    • 0025735778 scopus 로고
    • Molecular analysis of a human interferon-inducible gene family
    • Lewin, A. R.; Reid, L. E.; McMahon, M.; Stark, G. R.; Kerr, I. M. Molecular analysis of a human interferon-inducible gene family. Eur. J. Biochem. 1991, 199 (2), 417-423.
    • (1991) Eur. J. Biochem , vol.199 , Issue.2 , pp. 417-423
    • Lewin, A.R.1    Reid, L.E.2    McMahon, M.3    Stark, G.R.4    Kerr, I.M.5
  • 20
    • 0037092503 scopus 로고    scopus 로고
    • Integral membrane protein biosynthesis: Why topology is hard to predict
    • Ott, C. M.; Iingappa, V. R. Integral membrane protein biosynthesis: why topology is hard to predict. J. Cell Sci. 2002, 115 (Pt. 10), 2003- 2009.
    • (2002) J. Cell Sci , vol.115 , Issue.PART. 10 , pp. 2003-2009
    • Ott, C.M.1    Iingappa, V.R.2
  • 21
    • 25644458666 scopus 로고    scopus 로고
    • Automated electron microscope tomography using robust prediction of specimen movements
    • Mastronarde, D. N. Automated electron microscope tomography using robust prediction of specimen movements. J. Struct. Biol. 2005, 152 (1), 36-51.
    • (2005) J. Struct. Biol , vol.152 , Issue.1 , pp. 36-51
    • Mastronarde, D.N.1
  • 22
    • 0029879295 scopus 로고    scopus 로고
    • Kremer, 1. R.; Mastronarde, D. N.; Mcintosh, J. R. Computer visualization of three-dimensional image data using IMOD. J. Struct. Biol. 1996, 116 (1), 71-76.
    • Kremer, 1. R.; Mastronarde, D. N.; Mcintosh, J. R. Computer visualization of three-dimensional image data using IMOD. J. Struct. Biol. 1996, 116 (1), 71-76.
  • 24
    • 0036828724 scopus 로고    scopus 로고
    • Probability-based validation of protein identifications using a modified SEQUEST algorithm
    • MacCoss, M. J.; Wu, C. C.; Yates, J. R., III. Probability-based validation of protein identifications using a modified SEQUEST algorithm. Anal. Chem. 2002, 74 (21), 5593-5599.
    • (2002) Anal. Chem , vol.74 , Issue.21 , pp. 5593-5599
    • MacCoss, M.J.1    Wu, C.C.2    Yates III, J.R.3
  • 25
    • 0032953154 scopus 로고    scopus 로고
    • Enhancement of cyanogen bromide cleavage yields for methionyl-serine and methionyl-threonine peptide bonds
    • Kaiser, R.; Metzka, L. Enhancement of cyanogen bromide cleavage yields for methionyl-serine and methionyl-threonine peptide bonds. Anal. Biochem. 1999, 266 (1), 1-8.
    • (1999) Anal. Biochem , vol.266 , Issue.1 , pp. 1-8
    • Kaiser, R.1    Metzka, L.2
  • 26
    • 0036393898 scopus 로고    scopus 로고
    • DTASelect and Contrast: Tools for assembling and comparing protein identifications from shotgun proteomics
    • Tabb, D. L.; McDonald, W. H.; Yates, J. R., III. DTASelect and Contrast: tools for assembling and comparing protein identifications from shotgun proteomics. J. Proteome Res. 2002, 1 (1), 21- 26.
    • (2002) J. Proteome Res , vol.1 , Issue.1 , pp. 21-26
    • Tabb, D.L.1    McDonald, W.H.2    Yates III, J.R.3
  • 27
    • 33144485563 scopus 로고    scopus 로고
    • Quantitative comparison of proteomic data quality between a 2D and 3D quadrupole ion trap
    • Blackler, A. R.; Klammer, A. A.; MacCoss, M. J.; Wu, C. C. Quantitative comparison of proteomic data quality between a 2D and 3D quadrupole ion trap. Anal. Chem. 2006, 78 (4), 1337-1344.
    • (2006) Anal. Chem , vol.78 , Issue.4 , pp. 1337-1344
    • Blackler, A.R.1    Klammer, A.A.2    MacCoss, M.J.3    Wu, C.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.